Biological molecules

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46 Terms

1
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what is a monomer?

  • single unit which join together to form larger molecules

2
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what reaction joins two monomers together?

  • condensation reaction

  • Molecule of water produced

3
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what reaction breaks a chemical bond between two monomers?

  • hydrolysis

  • Use of a water molecule

4
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what is the name of monomers in a carbohydrate?

  • monosaccharide

5
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What are the different monosaccharides?

  • glucose

  • Fructose

  • Galactose

6
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name the different disaccharides and what they are made of:

  • Maltose: condensation of two glucose molecules

  • Sucrose: condensation of glucose and fructose molecules

  • Lactose: condensation of glucose and galactose molecules

7
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where is the OH group on the isomers of glucose?

  • OH above plane on beta (opposite)

  • OH below plan on alpha (together)

8
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What sort of bond is created between two monosaccharides?

glycosidic bond

9
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what are polymers of alpha glucose?

  • glycogen and starch are formed by condensation of alpha glucose

  • Coiled chains

  • Insoluble and doesn’t effect water potential

  • Large and compact

  • Branched and has more ends to be acted on at one given time by enzymes

  • Contains 1,6 bonding

  • All glucose are the same way up

  • No fibres

10
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what is the polymer for beta glucose?

  • cellulose formed by condensation of beta glucose

  • Forms straight unbranched chains

  • Unbranched chains run parallel to one another to form hydrogen bonds

  • Contains only 1,4 bonds

  • Alternating glucose

  • Contains fibres

11
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test for reducing sugar:

  • equal parts Benedikt’s solution

  • Heat gently for 5 minutes

  • Blue to brick red

12
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Test for non reducing sugar:

  • Benedikt’s test has to be negative

  • Add HCl then heat gently (hydrolyses dissacharides)

  • Add sodium hydrogencarbonate and test with pH paper to check it is alkaline

  • Add benedikt’s solution and heat

  • Blue to brick red

13
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Test for starch:

  • iodine test

  • Yellow to black

14
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what property of water results in the high temperature required to heat water?

  • specific heat capacity of water

  • Water molecules form hydrogen bonds

  • More energy needed to separate molecules of water

  • Requires more energy to heat a mass of water

  • Boiling point is higher than expected

  • Water is a buffer against sudden changes in temperature

  • Good for making aquatic environments temperature-stable

  • Good against sudden temperature changes for organisms in terrestrial environments as organisms are made up of water

15
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which property of water results in the large amount of energy required to vapourise water?

  • latent heat of vaporisation of water

  • Large amount of energy required to evaporate 1 gram of water

  • Evaporation is an effective way to cool down as it requires body heat to evaporate water

16
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Which property of water allows it to go up straws?

  • cohesion

  • Water has large cohesive forces so they can be pulled through tubes like xylem vessels

  • Water molecules tend to pull back into a body of water

  • Forms surface tension and water surface acts like skin

17
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what is the importance of water?

  • makes up organisms

  • Is an environment

  • Breaks down complex molecules during hydrolysis

  • Chemical reactions take place in water

  • Major material in photosynthesis

  • Solvent for gase

  • Provides structural support

  • Transparent so aquatic plants can photosynthesise

18
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What is the importance of lipids?

  • source of energy

  • Waterproofing

  • Insulation

  • Protection

19
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structure of triglycerides:

  • three fatty acid chains combined with three glycerol molecules

  • Ester bond formed between chain and glycerol by condensation reaction

  • Fatty acid chains have carboxyl group and a hydrocarbon chain (R group)

  • Unsaturated means there is a double carbon bond in thee chain, therefore cannot be packed together so closely making them liquid at room temp

20
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Properties of triglycerides:

  • high ratio of energy-storing C-H bonds to carbon atoms, excellent source of energy

  • Have low mass to energy ratio, good storage molecules

  • Large and non-polar, insoluble in water

21
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Structure of phospholipids:

  • One phosphate molecule and two fatty acid-glycerol chain

  • Phosphate molecule is hydrophilic

  • Forms polar molecule

22
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test for lipid

  • add sample being tested then ethanol

  • Shake tube

  • Add water

  • Shake tube

  • Water forms cloudy white emulsion

23
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What is the monomer of proteins?

amino acids

24
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Structure of amino acid:

  • central carbon

  • NH2 (amine) group

  • COOH (carboxyl group)

  • H

  • R group

25
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What bond is formed between amino acids?

  • peptide bond formed by condensation reaction

  • Polypeptides = formation of multiple amino acids by condensation

26
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Structure of proteins:

  • primary- formation of polypeptide from sequence of amino acids

  • Secondary- forming hydrogen bonds, creating helix 3D shaope

  • Tertiary- disulfide bridges, ionic bonds, hydrogen bond results in further folding

  • Quaternary- multiple polypeptide chains joining together

27
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what is the test for proteins?

  • biuret test, detects peptide bonds

  • Add biuret reagent

  • Blue to purple colour change

28
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definition of enzyme:

  • proteins that act as a catalyst in reactions

29
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use of enzyme:

  • speeds up reaction by lowering activation energy without being used up itself

30
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describe the induced fit model of enzymes:

  • Substrate binds to active site of enzyme

  • Forming enzyme-substrate complex

  • Active site changes shape so it is complementary to substrate

  • Distorts bonds in substrate

  • Reduces activation energy

31
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what are enzyme inhibitors?

  • substances that either directly or indirectly interferes with functioning of the active site of an enzyme, reducing its activity

32
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Competitive inhibitors:

  • have molecular shape similar o substrate

  • Occupies the active site of enzyme

  • Competes with substrate for available active site

  • reduces rate of reaction, however the reaction will still occur in full

33
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non-competitive inhibitors:

  • non-competitive inhibitors attach themselves to enzyme at binding site which is NOT active site

  • Inhibitor alters shape on enzyme and so changes shape of alive site

  • Substrate can no longer bind to enzyme

34
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Structure of a nuclotide:

  • pentose sugar

  • Phosphate group

  • Nitrogenous base (uracil, thymine, guanine, cytosine, adenine)

  • All joined together by condensation reaction

35
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how are polynucleotides made?

  • condensation reaction between phosphate group of one nucleotide and pentose sugar of another

  • Forms phosphodiester bond

36
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difference between RNA and DNA structure:

  • DNA has two strands RNA has one

  • DNA contains deoxyribose pentose sugar RNA contains ribose pentose sugar

  • DNA has bases T,A,C,G RNA has bases A,U,C,G

  • DNA bases form hydrogen bonds RNA doesn’t

37
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how is the DNA stable?

  • phosphodiester backbone protects more chemically reactive organic bases within double helix

  • Hydrogen bonds between organic bases forms bridges

  • Three hydrogen bonds between C-G, so more CG pairings the more stable it is

38
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describe semi-conservative replication:

  • enzyme DNA helicase breaks hydrogen bond linking base pairs of DNA

  • Double helix unwinds to form two strands

  • One strand used as template strand

  • Free nucleotides with bases complementary to exposed nucleotide bind

  • DNA polymerase joins free nucleotides together by a condensation reaction

  • each new DNA molecule contains one of the original DNA strand

39
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what requirements are there for semi conservative repication?

  • four types of nucleotide with bases complementary pairs

  • Both strands of DNA acting as templates for attachment of nucleotide

  • Enzyme DNA polymerase

  • Source of chemical energy to drive process

40
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who came up with the idea of semi-conservative replication?

  • watson and crick

41
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Structure of ATP:

  • adenine base

  • Ribose sugar

  • Three phosphate groups

42
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How does ATP store energy?

  • bond between phosphate groups are unstable and have low activation energy

  • When bonds are broken they release a considerable amount of energy

  • Usually on the terminal phosphate is removed

  • ATP + H2O —> ADP + Pi + E (energy)

  • Hydrolysis reaction as it uses a molecule of water

43
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Describe synthesis of ATP:

  • ADP re-forms to ATP by adding phosphate groups

  • Catalysed by enzyme ATP synthase

  • Condensation reaction as it produces a water molecule

44
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When does synthesis of ATP occur?

  • in chlorophyll-containing plant cells during photosynthesis photophosphorylation

  • In plant and animal cells during respiration oxidative phosphorylation

  • in plant and animal cells when phosphate groups are transferred from donor molecules to ADP substrate-level phosphorylation

45
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roles of ATP:

  • metabolic process

  • Movement

  • Active transport

  • Secretion

  • Activation of molecules

46
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Why is ATP an immediate energy source?

  • good energy donor but not a good long-term storage of energy

  • Therefore not stored in large quantities as ADP forms into ATP very quickly